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Database: UniProt
Entry: A0A2K5Z5V7_MANLE
LinkDB: A0A2K5Z5V7_MANLE
Original site: A0A2K5Z5V7_MANLE 
ID   A0A2K5Z5V7_MANLE        Unreviewed;       102 AA.
AC   A0A2K5Z5V7;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Histone H2A {ECO:0000256|RuleBase:RU003767};
GN   Name=H2AZ2 {ECO:0000313|Ensembl:ENSMLEP00000023211.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000023211.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000023211.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Variant histone H2A which replaces conventional H2A in a
CC       subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin,
CC       limiting DNA accessibility to the cellular machineries which require
CC       DNA as a template. Histones thereby play a central role in
CC       transcription regulation, DNA repair, DNA replication and chromosomal
CC       stability. DNA accessibility is regulated via a complex set of post-
CC       translational modifications of histones, also called histone code, and
CC       nucleosome remodeling. May be involved in the formation of constitutive
CC       heterochromatin. May be required for chromosome segregation during cell
CC       division. {ECO:0000256|ARBA:ARBA00037205}.
CC   -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC       each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC       two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of
CC       DNA. {ECO:0000256|RuleBase:RU003767}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU003767}.
CC   -!- SIMILARITY: Belongs to the histone H2A family.
CC       {ECO:0000256|RuleBase:RU003767}.
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DR   RefSeq; XP_011838655.1; XM_011983265.1.
DR   AlphaFoldDB; A0A2K5Z5V7; -.
DR   SMR; A0A2K5Z5V7; -.
DR   Ensembl; ENSMLET00000046725.1; ENSMLEP00000023211.1; ENSMLEG00000035764.1.
DR   GeneID; 105541954; -.
DR   GeneTree; ENSGT00900000140979; -.
DR   OrthoDB; 235643at2759; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   CDD; cd00074; H2A; 1.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR002119; Histone_H2A.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   InterPro; IPR032454; Histone_H2A_C.
DR   PANTHER; PTHR23430; HISTONE H2A; 1.
DR   PANTHER; PTHR23430:SF280; HISTONE H2A.V; 1.
DR   Pfam; PF00125; Histone; 1.
DR   Pfam; PF16211; Histone_H2A_C; 1.
DR   PRINTS; PR00620; HISTONEH2A.
DR   SMART; SM00414; H2A; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
PE   3: Inferred from homology;
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU003767};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU003767};
KW   Nucleosome core {ECO:0000256|ARBA:ARBA00023269,
KW   ECO:0000256|RuleBase:RU003767}; Nucleus {ECO:0000256|RuleBase:RU003767};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          2..67
FT                   /note="Histone H2A/H2B/H3"
FT                   /evidence="ECO:0000259|Pfam:PF00125"
FT   DOMAIN          69..101
FT                   /note="Histone H2A C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16211"
SQ   SEQUENCE   102 AA;  10999 MW;  0E6071539B4139F9 CRC64;
     MFPVGRIHRH LKTRTTSHGR VGATAAVYSA AILEYLTAEV LELAGNASKD LKVKRITPRH
     LQLAIRGDEE LDSLIKATIA GGGVIPHIHK SLIGKKGQQK TA
//
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